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Database: PDB
Entry: 4FDC
LinkDB: 4FDC
Original site: 4FDC 
HEADER    APOPTOSIS, OXIDOREDUCTASE               27-MAY-12   4FDC              
TITLE     CRYSTAL STRUCTURE OF THE E493V MUTANT OF HUMAN APOPTOSIS INDUCING     
TITLE    2 FACTOR (AIF)                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS-INDUCING FACTOR 1, MITOCHONDRIAL;                
COMPND   3 CHAIN: B;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 103-613;                                      
COMPND   5 SYNONYM: PROGRAMMED CELL DEATH PROTEIN 8;                            
COMPND   6 EC: 1.-.-.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AIF, AIFM1, PDCD8;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PKK                                       
KEYWDS    ROSSMANN FOLD, MITOCHONDRION, APPOPTOSIS,OXIDOREDUCTASE, APOPTOSIS,   
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.F.SEVRIOUKOVA                                                       
REVDAT   2   02-JAN-13 4FDC    1       JRNL                                     
REVDAT   1   17-OCT-12 4FDC    0                                                
JRNL        AUTH   C.RINALDI,C.GRUNSEICH,I.F.SEVRIOUKOVA,A.SCHINDLER,           
JRNL        AUTH 2 I.HORKAYNE-SZAKALY,C.LAMPERTI,G.LANDOURE,M.L.KENNERSON,      
JRNL        AUTH 3 B.G.BURNETT,C.BONNEMANN,L.G.BIESECKER,D.GHEZZI,M.ZEVIANI,    
JRNL        AUTH 4 K.H.FISCHBECK                                                
JRNL        TITL   COWCHOCK SYNDROME IS ASSOCIATED WITH A MUTATION IN           
JRNL        TITL 2 APOPTOSIS-INDUCING FACTOR.                                   
JRNL        REF    AM.J.HUM.GENET.               V.  91  1095 2012              
JRNL        REFN                   ISSN 0002-9297                               
JRNL        PMID   23217327                                                     
JRNL        DOI    10.1016/J.AJHG.2012.10.008                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 20005                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.255                           
REMARK   3   R VALUE            (WORKING SET) : 0.253                           
REMARK   3   FREE R VALUE                     : 0.297                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1082                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1308                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3555                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 53                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 84.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 130.22                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.56000                                             
REMARK   3    B22 (A**2) : 0.50000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.08000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.395         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.314         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.305         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.854        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.901                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3674 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4976 ; 1.185 ; 1.982       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   459 ; 5.858 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   154 ;34.723 ;23.442       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   628 ;17.126 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;15.941 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   551 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2747 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   128        B   610                          
REMARK   3    RESIDUE RANGE :   B  1000        B  1000                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.8306   2.6970 -25.6071              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3690 T22:   0.3401                                     
REMARK   3      T33:   0.2269 T12:  -0.2934                                     
REMARK   3      T13:  -0.0224 T23:   0.0879                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9765 L22:   0.8914                                     
REMARK   3      L33:   0.9080 L12:   1.1860                                     
REMARK   3      L13:   0.4006 L23:  -0.0266                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5413 S12:   0.6170 S13:   0.1801                       
REMARK   3      S21:  -0.2498 S22:   0.4488 S23:   0.0845                       
REMARK   3      S31:  -0.0338 S32:   0.0268 S33:   0.0925                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4FDC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072758.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 103                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20005                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.45000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.46                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1M6I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 1500, 0.1 M TRISHCL PH 8.5, 4%   
REMARK 280  ACETONE, MICROBATCH UNDER OIL, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       51.20000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       51.20000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.35000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B   103                                                      
REMARK 465     LEU B   104                                                      
REMARK 465     THR B   105                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     GLU B   107                                                      
REMARK 465     GLN B   108                                                      
REMARK 465     LYS B   109                                                      
REMARK 465     GLN B   110                                                      
REMARK 465     LYS B   111                                                      
REMARK 465     LYS B   112                                                      
REMARK 465     ALA B   113                                                      
REMARK 465     ALA B   114                                                      
REMARK 465     LEU B   115                                                      
REMARK 465     SER B   116                                                      
REMARK 465     ALA B   117                                                      
REMARK 465     SER B   118                                                      
REMARK 465     GLU B   119                                                      
REMARK 465     GLY B   120                                                      
REMARK 465     GLU B   121                                                      
REMARK 465     GLU B   122                                                      
REMARK 465     VAL B   123                                                      
REMARK 465     PRO B   124                                                      
REMARK 465     GLN B   125                                                      
REMARK 465     ASP B   126                                                      
REMARK 465     LYS B   127                                                      
REMARK 465     ALA B   538                                                      
REMARK 465     SER B   539                                                      
REMARK 465     GLU B   540                                                      
REMARK 465     ILE B   541                                                      
REMARK 465     THR B   542                                                      
REMARK 465     ILE B   543                                                      
REMARK 465     PRO B   544                                                      
REMARK 465     PRO B   545                                                      
REMARK 465     SER B   546                                                      
REMARK 465     THR B   547                                                      
REMARK 465     PRO B   548                                                      
REMARK 465     ALA B   549                                                      
REMARK 465     VAL B   550                                                      
REMARK 465     PRO B   551                                                      
REMARK 465     GLN B   552                                                      
REMARK 465     ALA B   553                                                      
REMARK 465     PRO B   554                                                      
REMARK 465     VAL B   555                                                      
REMARK 465     GLN B   556                                                      
REMARK 465     GLY B   557                                                      
REMARK 465     GLU B   558                                                      
REMARK 465     ASP B   559                                                      
REMARK 465     HIS B   611                                                      
REMARK 465     GLU B   612                                                      
REMARK 465     ASP B   613                                                      
REMARK 465     LEU B   614                                                      
REMARK 465     VAL B   615                                                      
REMARK 465     PRO B   616                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP B   417     NH2  ARG B   449              1.63            
REMARK 500   O    ALA B   407     CG   GLU B   413              1.92            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO B 155        4.99    -59.40                                   
REMARK 500    LYS B 177     -123.90   -127.16                                   
REMARK 500    GLN B 195     -177.30    -68.69                                   
REMARK 500    ASN B 222      -11.48     75.50                                   
REMARK 500    ARG B 285      -32.21   -156.25                                   
REMARK 500    SER B 376       36.77     74.51                                   
REMARK 500    LEU B 406       11.29    -64.37                                   
REMARK 500    LYS B 408      -62.72    -91.91                                   
REMARK 500    GLU B 413       51.85     12.64                                   
REMARK 500    ILE B 414      176.82     55.07                                   
REMARK 500    ASP B 415     -114.71   -100.84                                   
REMARK 500    SER B 416      -63.06   -179.01                                   
REMARK 500    ALA B 472     -147.58    155.22                                   
REMARK 500    LEU B 486       71.51   -108.57                                   
REMARK 500    THR B 512     -159.90    -95.81                                   
REMARK 500    ASP B 515       48.33    -96.72                                   
REMARK 500    THR B 534      161.73     71.90                                   
REMARK 500    ASP B 570     -115.23     66.71                                   
REMARK 500    ASP B 600      -89.19   -122.06                                   
REMARK 500    LEU B 601      -26.83    107.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU B 413        24.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1000                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1M6I   RELATED DB: PDB                                   
REMARK 900 WILD TYPE HUMAN AIF                                                  
DBREF  4FDC B  103   613  UNP    O95831   AIFM1_HUMAN    103    613             
SEQADV 4FDC VAL B  493  UNP  O95831    GLU   493 ENGINEERED MUTATION            
SEQADV 4FDC LEU B  614  UNP  O95831              EXPRESSION TAG                 
SEQADV 4FDC VAL B  615  UNP  O95831              EXPRESSION TAG                 
SEQADV 4FDC PRO B  616  UNP  O95831              EXPRESSION TAG                 
SEQRES   1 B  514  GLY LEU THR PRO GLU GLN LYS GLN LYS LYS ALA ALA LEU          
SEQRES   2 B  514  SER ALA SER GLU GLY GLU GLU VAL PRO GLN ASP LYS ALA          
SEQRES   3 B  514  PRO SER HIS VAL PRO PHE LEU LEU ILE GLY GLY GLY THR          
SEQRES   4 B  514  ALA ALA PHE ALA ALA ALA ARG SER ILE ARG ALA ARG ASP          
SEQRES   5 B  514  PRO GLY ALA ARG VAL LEU ILE VAL SER GLU ASP PRO GLU          
SEQRES   6 B  514  LEU PRO TYR MET ARG PRO PRO LEU SER LYS GLU LEU TRP          
SEQRES   7 B  514  PHE SER ASP ASP PRO ASN VAL THR LYS THR LEU ARG PHE          
SEQRES   8 B  514  LYS GLN TRP ASN GLY LYS GLU ARG SER ILE TYR PHE GLN          
SEQRES   9 B  514  PRO PRO SER PHE TYR VAL SER ALA GLN ASP LEU PRO HIS          
SEQRES  10 B  514  ILE GLU ASN GLY GLY VAL ALA VAL LEU THR GLY LYS LYS          
SEQRES  11 B  514  VAL VAL GLN LEU ASP VAL ARG ASP ASN MET VAL LYS LEU          
SEQRES  12 B  514  ASN ASP GLY SER GLN ILE THR TYR GLU LYS CYS LEU ILE          
SEQRES  13 B  514  ALA THR GLY GLY THR PRO ARG SER LEU SER ALA ILE ASP          
SEQRES  14 B  514  ARG ALA GLY ALA GLU VAL LYS SER ARG THR THR LEU PHE          
SEQRES  15 B  514  ARG LYS ILE GLY ASP PHE ARG SER LEU GLU LYS ILE SER          
SEQRES  16 B  514  ARG GLU VAL LYS SER ILE THR ILE ILE GLY GLY GLY PHE          
SEQRES  17 B  514  LEU GLY SER GLU LEU ALA CYS ALA LEU GLY ARG LYS ALA          
SEQRES  18 B  514  ARG ALA LEU GLY THR GLU VAL ILE GLN LEU PHE PRO GLU          
SEQRES  19 B  514  LYS GLY ASN MET GLY LYS ILE LEU PRO GLU TYR LEU SER          
SEQRES  20 B  514  ASN TRP THR MET GLU LYS VAL ARG ARG GLU GLY VAL LYS          
SEQRES  21 B  514  VAL MET PRO ASN ALA ILE VAL GLN SER VAL GLY VAL SER          
SEQRES  22 B  514  SER GLY LYS LEU LEU ILE LYS LEU LYS ASP GLY ARG LYS          
SEQRES  23 B  514  VAL GLU THR ASP HIS ILE VAL ALA ALA VAL GLY LEU GLU          
SEQRES  24 B  514  PRO ASN VAL GLU LEU ALA LYS THR GLY GLY LEU GLU ILE          
SEQRES  25 B  514  ASP SER ASP PHE GLY GLY PHE ARG VAL ASN ALA GLU LEU          
SEQRES  26 B  514  GLN ALA ARG SER ASN ILE TRP VAL ALA GLY ASP ALA ALA          
SEQRES  27 B  514  CYS PHE TYR ASP ILE LYS LEU GLY ARG ARG ARG VAL GLU          
SEQRES  28 B  514  HIS HIS ASP HIS ALA VAL VAL SER GLY ARG LEU ALA GLY          
SEQRES  29 B  514  GLU ASN MET THR GLY ALA ALA LYS PRO TYR TRP HIS GLN          
SEQRES  30 B  514  SER MET PHE TRP SER ASP LEU GLY PRO ASP VAL GLY TYR          
SEQRES  31 B  514  VAL ALA ILE GLY LEU VAL ASP SER SER LEU PRO THR VAL          
SEQRES  32 B  514  GLY VAL PHE ALA LYS ALA THR ALA GLN ASP ASN PRO LYS          
SEQRES  33 B  514  SER ALA THR GLU GLN SER GLY THR GLY ILE ARG SER GLU          
SEQRES  34 B  514  SER GLU THR GLU SER GLU ALA SER GLU ILE THR ILE PRO          
SEQRES  35 B  514  PRO SER THR PRO ALA VAL PRO GLN ALA PRO VAL GLN GLY          
SEQRES  36 B  514  GLU ASP TYR GLY LYS GLY VAL ILE PHE TYR LEU ARG ASP          
SEQRES  37 B  514  LYS VAL VAL VAL GLY ILE VAL LEU TRP ASN ILE PHE ASN          
SEQRES  38 B  514  ARG MET PRO ILE ALA ARG LYS ILE ILE LYS ASP GLY GLU          
SEQRES  39 B  514  GLN HIS GLU ASP LEU ASN GLU VAL ALA LYS LEU PHE ASN          
SEQRES  40 B  514  ILE HIS GLU ASP LEU VAL PRO                                  
HET    FAD  B1000      53                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
HELIX    1   1 GLY B  140  ASP B  154  1                                  15    
HELIX    2   2 ARG B  172  PHE B  181  5                                  10    
HELIX    3   3 ASN B  186  LEU B  191  1                                   6    
HELIX    4   4 PRO B  207  TYR B  211  5                                   5    
HELIX    5   5 LEU B  267  ARG B  272  1                                   6    
HELIX    6   6 GLY B  274  SER B  279  1                                   6    
HELIX    7   7 LYS B  286  VAL B  300  1                                  15    
HELIX    8   8 GLY B  309  GLY B  327  1                                  19    
HELIX    9   9 PRO B  345  GLU B  359  1                                  15    
HELIX   10  10 VAL B  404  LYS B  408  5                                   5    
HELIX   11  11 HIS B  454  THR B  470  1                                  17    
HELIX   12  12 ASN B  516  GLY B  525  1                                  10    
HELIX   13  13 ILE B  528  GLU B  533  1                                   6    
HELIX   14  14 ARG B  584  GLY B  595  1                                  12    
HELIX   15  15 LEU B  601  LEU B  607  1                                   7    
SHEET    1   A 6 GLY B 224  THR B 229  0                                        
SHEET    2   A 6 ARG B 158  SER B 163  1  N  ILE B 161   O  ALA B 226           
SHEET    3   A 6 HIS B 131  ILE B 137  1  N  LEU B 136   O  LEU B 160           
SHEET    4   A 6 GLN B 250  ILE B 258  1  O  LYS B 255   N  PRO B 133           
SHEET    5   A 6 MET B 242  LEU B 245 -1  N  VAL B 243   O  ILE B 251           
SHEET    6   A 6 VAL B 233  ASP B 237 -1  N  VAL B 234   O  LYS B 244           
SHEET    1   B 6 GLY B 224  THR B 229  0                                        
SHEET    2   B 6 ARG B 158  SER B 163  1  N  ILE B 161   O  ALA B 226           
SHEET    3   B 6 HIS B 131  ILE B 137  1  N  LEU B 136   O  LEU B 160           
SHEET    4   B 6 GLN B 250  ILE B 258  1  O  LYS B 255   N  PRO B 133           
SHEET    5   B 6 ILE B 433  VAL B 435  1  O  TRP B 434   N  CYS B 256           
SHEET    6   B 6 GLN B 428  ARG B 430 -1  N  ALA B 429   O  ILE B 433           
SHEET    1   C 2 ARG B 192  LYS B 194  0                                        
SHEET    2   C 2 GLU B 200  SER B 202 -1  O  ARG B 201   N  PHE B 193           
SHEET    1   D 2 GLY B 262  PRO B 264  0                                        
SHEET    2   D 2 LEU B 400  PRO B 402 -1  O  GLU B 401   N  THR B 263           
SHEET    1   E 5 THR B 281  LEU B 283  0                                        
SHEET    2   E 5 HIS B 393  ALA B 396  1  O  ALA B 396   N  THR B 282           
SHEET    3   E 5 SER B 302  ILE B 306  1  N  THR B 304   O  HIS B 393           
SHEET    4   E 5 GLU B 329  LEU B 333  1  O  ILE B 331   N  ILE B 305           
SHEET    5   E 5 LYS B 362  MET B 364  1  O  MET B 364   N  GLN B 332           
SHEET    1   F 3 VAL B 369  VAL B 374  0                                        
SHEET    2   F 3 LEU B 379  LEU B 383 -1  O  LYS B 382   N  GLN B 370           
SHEET    3   F 3 LYS B 388  THR B 391 -1  O  THR B 391   N  LEU B 379           
SHEET    1   G 3 PHE B 421  ARG B 422  0                                        
SHEET    2   G 3 ALA B 440  ASP B 444  1  O  CYS B 441   N  PHE B 421           
SHEET    3   G 3 GLY B 448  ARG B 451 -1  O  GLY B 448   N  ASP B 444           
SHEET    1   H 5 PHE B 482  ASP B 485  0                                        
SHEET    2   H 5 GLY B 491  GLY B 496 -1  O  TYR B 492   N  SER B 484           
SHEET    3   H 5 VAL B 572  TRP B 579 -1  O  LEU B 578   N  VAL B 493           
SHEET    4   H 5 LYS B 562  ARG B 569 -1  N  GLY B 563   O  TRP B 579           
SHEET    5   H 5 THR B 504  ALA B 509 -1  N  VAL B 505   O  PHE B 566           
CISPEP   1 GLY B  471    ALA B  472          0         5.43                     
SITE     1 AC1 25 GLY B 138  GLY B 139  GLY B 140  THR B 141                    
SITE     2 AC1 25 ALA B 142  VAL B 162  GLU B 164  ARG B 172                    
SITE     3 AC1 25 PRO B 173  SER B 176  LYS B 177  LYS B 232                    
SITE     4 AC1 25 VAL B 233  ALA B 259  THR B 260  GLY B 261                    
SITE     5 AC1 25 ARG B 285  LEU B 311  GLY B 437  ASP B 438                    
SITE     6 AC1 25 GLU B 453  HIS B 454  HIS B 455  PHE B 482                    
SITE     7 AC1 25 TRP B 483                                                     
CRYST1  102.400   62.700  101.922  90.00 118.57  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009766  0.000000  0.005318        0.00000                         
SCALE2      0.000000  0.015949  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011172        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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